TY - JOUR
T1 - A comprehensive evaluation of the activity and selectivity profile of ligands for RGD-binding integrins
AU - Kapp, Tobias G.
AU - Rechenmacher, Florian
AU - Neubauer, Stefanie
AU - Maltsev, Oleg V.
AU - Cavalcanti-Adam, Elisabetta A.
AU - Zarka, Revital
AU - Reuning, Ute
AU - Notni, Johannes
AU - Wester, Hans Jürgen
AU - Mas-Moruno, Carlos
AU - Spatz, Joachim
AU - Geiger, Benjamin
AU - Kessler, Horst
N1 - Publisher Copyright:
© The Author(s) 2017.
PY - 2017/1/11
Y1 - 2017/1/11
N2 - Integrins, a diverse class of heterodimeric cell surface receptors, are key regulators of cell structure and behaviour, affecting cell morphology, proliferation, survival and differentiation. Consequently, mutations in specific integrins, or their deregulated expression, are associated with a variety of diseases. In the last decades, many integrin-specific ligands have been developed and used for modulation of integrin function in medical as well as biophysical studies. The IC 50 -values reported for these ligands strongly vary and are measured using different cell-based and cell-free systems. A systematic comparison of these values is of high importance for selecting the optimal ligands for given applications. In this study, we evaluate a wide range of ligands for their binding affinity towards the RGD-binding integrins αvβ3, αvβ5, αvβ6, αvβ8, α5β1, αIIbβ3, using homogenous ELISA-like solid phase binding assay.
AB - Integrins, a diverse class of heterodimeric cell surface receptors, are key regulators of cell structure and behaviour, affecting cell morphology, proliferation, survival and differentiation. Consequently, mutations in specific integrins, or their deregulated expression, are associated with a variety of diseases. In the last decades, many integrin-specific ligands have been developed and used for modulation of integrin function in medical as well as biophysical studies. The IC 50 -values reported for these ligands strongly vary and are measured using different cell-based and cell-free systems. A systematic comparison of these values is of high importance for selecting the optimal ligands for given applications. In this study, we evaluate a wide range of ligands for their binding affinity towards the RGD-binding integrins αvβ3, αvβ5, αvβ6, αvβ8, α5β1, αIIbβ3, using homogenous ELISA-like solid phase binding assay.
UR - http://www.scopus.com/inward/record.url?scp=85009223915&partnerID=8YFLogxK
U2 - 10.1038/srep39805
DO - 10.1038/srep39805
M3 - Article
C2 - 28074920
AN - SCOPUS:85009223915
VL - 7
JO - Scientific Reports
JF - Scientific Reports
M1 - 39805
ER -